Trends in the development of innovative nanobiocatalysts and their application in biocatalytic transformations

Gkantzou, Elena; Chatzikonstantinou, Alexandra V.; Fotiadou, Renia; Giannakopoulou, Αrchontoula; Patila, Michaela; Stamatis, Haralambos

doi:10.1016/j.biotechadv.2021.107738

Cited by 61 publications

(49 citation statements)

References 273 publications

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“…The biosensor is defined as an analytical device in which the biological system (e.g., enzymes, receptors, antibodies, microorganisms, or cells) meets the sample analyte and transforms it into either an electric signal, an optical signal, a thermal signal, or another kind of signal [15,[35][36][37][38][39]. The amplitude of the generated signal is directly related to the concentration of analytes in the solution.…”

Section: Structure Of Typical Laccase-based Biosensorsmentioning

confidence: 99%

Recent Advances in the Development of Laccase-Based Biosensors via Nano-Immobilization Techniques

et al. 2022

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Monitoring phenolic compounds is critical in the environmental, food, and medical sectors. Among many recent advanced detection platforms, laccase-based biosensing platforms gave very rapid, effective, online, and in situ sensing of phenolic compounds. In laccase-based biosensors, laccase immobilization techniques have a vital role. However, a detailing of the advancements in laccase immobilization techniques employed in laccase-based biosensors is lacking in the literature. Thus, in this review, we assessed how the nano-immobilization techniques shaped the laccase biosensing platforms. We discussed novel developments in laccase immobilization techniques such as entrapment, adsorption, cross-linking, and covalent over new nanocomposites in laccase biosensors. We made a comprehensive assessment based on the current literature for future perspectives of nano-immobilized laccase biosensors. We found the important key areas toward which future laccase biosensor research seems to be heading. These include 1. A focus on the development of multi-layer laccase over electrode surface, 2. The need to utilize more covalent immobilization routes, as they change the laccase specificity toward phenolic compounds, 3. The advancement in polymeric matrices with electroconductive properties, and 4. novel entrapment techniques like biomineralization using laccase molecules. Thus, in this review, we provided a detailed account of immobilization in laccase biosensors and their feasibility in the future for the development of highly specific laccase biosensors in industrial, medicinal, food, and environmental applications.

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Section: Structure Of Typical Laccase-based Biosensorsmentioning

confidence: 99%

Recent Advances in the Development of Laccase-Based Biosensors via Nano-Immobilization Techniques

et al. 2022

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“…Nanotechnology has given rise to new opportunities in different biotechnological field, particularly in enzymes field which have been used in the enhancement of enzyme catalytic activity, thermostability, reusability and many other characteristics through enzyme immobilization ( Rai et al, 2019 ; Gkantzou et al, 2021 ). The movement of enzymes at elevated temperature is limited by immobilization, which leads to enhanced stability of the enzyme.…”

Section: Strategies To Enhance Thermostability and Specific Activity Of Cellulase And Xylanase Of Thermophilesmentioning

confidence: 99%

Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

Ajeje¹,

Hu²,

Song³

et al. 2021

Front. Bioeng. Biotechnol.

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The bioconversion of lignocellulose into monosaccharides is critical for ensuring the continual manufacturing of biofuels and value-added bioproducts. Enzymatic degradation, which has a high yield, low energy consumption, and enhanced selectivity, could be the most efficient and environmentally friendly technique for converting complex lignocellulose polymers to fermentable monosaccharides, and it is expected to make cellulases and xylanases the most demanded industrial enzymes. The widespread nature of thermophilic microorganisms allows them to proliferate on a variety of substrates and release substantial quantities of cellulases and xylanases, which makes them a great source of thermostable enzymes. The most significant breakthrough of lignocellulolytic enzymes lies in lignocellulose-deconstruction by enzymatic depolymerization of holocellulose into simple monosaccharides. However, commercially valuable thermostable cellulases and xylanases are challenging to produce in high enough quantities. Thus, the present review aims at giving an overview of the most recent thermostable cellulases and xylanases isolated from thermophilic and hyperthermophilic microbes. The emphasis is on recent advancements in manufacturing these enzymes in other mesophilic host and enhancement of catalytic activity as well as thermostability of thermophilic cellulases and xylanases, using genetic engineering as a promising and efficient technology for its economic production. Additionally, the biotechnological applications of thermostable cellulases and xylanases of thermophiles were also discussed.

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“…The materials and general methods mentioned above have been exploited for coimmobilization of two or more enzymes in a single solid support for enzymatic onepot cascade reactions [12,15,16,26,[131][132][133]. Co-immobilization of enzymes is challenging since the co-immobilization method must be suitable for the different enzymes to be immobilized and control of the localization of different enzymes and activity ratio might be required for an efficient cascade.…”

Section: Thiol-disulphide Interchangementioning

confidence: 99%

Multicatalytic Hybrid Materials for Biocatalytic and Chemoenzymatic Cascades—Strategies for Multicatalyst (Enzyme) Co-Immobilization

et al. 2021

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During recent decades, the use of enzymes or chemoenzymatic cascades for organic chemistry has gained much importance in fundamental and industrial research. Moreover, several enzymatic and chemoenzymatic reactions have also served in green and sustainable manufacturing processes especially in fine chemicals, pharmaceutical, and flavor/fragrance industries. Unfortunately, only a few processes have been applied at industrial scale because of the low stabilities of enzymes along with the problematic processes of their recovery and reuse. Immobilization and co-immobilization offer an ideal solution to these problems. This review gives an overview of all the pathways for enzyme immobilization and their use in integrated enzymatic and chemoenzymatic processes in cascade or in a one-pot concomitant execution. We place emphasis on the factors that must be considered to understand the process of immobilization. A better understanding of this fundamental process is an essential tool not only in the choice of the best route of immobilization but also in the understanding of their catalytic activity.

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Trends in the development of innovative nanobiocatalysts and their application in biocatalytic transformations

Cited by 61 publications

References 273 publications

Recent Advances in the Development of Laccase-Based Biosensors via Nano-Immobilization Techniques

Recent Advances in the Development of Laccase-Based Biosensors via Nano-Immobilization Techniques

Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

Multicatalytic Hybrid Materials for Biocatalytic and Chemoenzymatic Cascades—Strategies for Multicatalyst (Enzyme) Co-Immobilization

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